Information on EC 1.14.17.3 - peptidylglycine monooxygenase

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The expected taxonomic range for this enzyme is: Eumetazoa

EC NUMBER
COMMENTARY
1.14.17.3
-
RECOMMENDED NAME
GeneOntology No.
peptidylglycine monooxygenase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
peptidylglycine + ascorbate + O2 = peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
mechanism
-
peptidylglycine + ascorbate + O2 = peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
mechanism
-
peptidylglycine + ascorbate + O2 = peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
mechanism
-
peptidylglycine + ascorbate + O2 = peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
sequential activity of 2 enzymes contained within a bifunctional protein
-
peptidylglycine + ascorbate + O2 = peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
equilibrium ordered mechanism
-
peptidylglycine + ascorbate + O2 = peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
kinetic model for slow-binding inhibition
-
peptidylglycine + ascorbate + O2 = peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
structural analysis of mutant H172A, binding of ligands CO, Cu2+
-
peptidylglycine + ascorbate + O2 = peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
structural analysis
-
peptidylglycine + ascorbate + O2 = peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
ping-pong-mechanism
-
peptidylglycine + ascorbate + O2 = peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
structure analysis
-
peptidylglycine + ascorbate + O2 = peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
A copper protein. Peptidylglycines with a neutral amino acid residue in the penultimate position are the best substrates for the enzyme. The product is unstable and dismutates to glyoxylate and the corresponding desglycine peptide amide, a reaction catalysed by EC 4.3.2.5 peptidylamidoglycolate lyase. Involved in the biosynthesis of alpha-melanotropin and related biologically active peptides.
-
-
-
peptidylglycine + ascorbate + O2 = peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
kinetic analysis
-
peptidylglycine + ascorbate + O2 = peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
bifunctional enzyme showing peptidylglycine alpha-hydroxylating monooxygenase, EC 1.14.17.3, and peptidylamidoglycolate lyase, PAL, EC 4.3.2.5, activities, the enzyme possesses 2 catalytic domains
-
peptidylglycine + ascorbate + O2 = peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
bifunctional enzyme showing peptidylglycine alpha-hydroxylating monooxygenase, EC 1.14.17.3, and peptidylamidoglycolate lyase, PAL, EC 4.3.2.5, activities, the enzyme possesses 2 catalytic domains
-
peptidylglycine + ascorbate + O2 = peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
bifunctional enzyme showing peptidylglycine alpha-hydroxylating monooxygenase, EC 1.14.17.3, and peptidylamidoglycolate lyase, PAL, EC 4.3.2.5, activities, the enzyme possesses 2 catalytic domains
P19021
peptidylglycine + ascorbate + O2 = peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
bifunctional enzyme showing peptidylglycine alpha-hydroxylating monooxygenase, PHM, EC 1.14.17.3, and peptidylamidoglycolate lyase, PAL, EC 4.3.2.5, activities
-
peptidylglycine + ascorbate + O2 = peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
cleavage of CN bond in N-acetylated glycines, R-CO-NH-CH2-COOH, e.g. found in neuropeptide prohormones
-
peptidylglycine + ascorbate + O2 = peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
detailed analysis of the reaction mechanism, reaction scheme, strictly ordered ping-pong kinetic mechanism in which ascorbate first reduces Cu(II) to Cu(I), semidehydroascorbate being released, after which the peptide binds and finally oxygen, active site structure
-
peptidylglycine + ascorbate + O2 = peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
detailed analysis of the reaction mechanism, role of noncoupled nature of the active site
-
peptidylglycine + ascorbate + O2 = peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
equilibrium-ordered and steady-state-random or -ordered reaction mechanism for the wild-type and the mutant Y318F enzyme, respectively, active site Y318 is involved, C-H bond activation is dominated by quantum mechanical tunneling, peptide substrate binding structure at the active site
-
peptidylglycine + ascorbate + O2 = peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
inter-copper electron transfer, interdomain structure
-
peptidylglycine + ascorbate + O2 = peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
mechanism, substrate binding structure
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
peptidylglycine,ascorbate:oxygen oxidoreductase (2-hydroxylating)
A copper protein. Peptidylglycines with a neutral amino acid residue in the penultimate position are the best substrates for the enzyme. The product is unstable and dismutates to glyoxylate and the corresponding desglycine peptide amide, a reaction catalysed by EC 4.3.2.5 peptidylamidoglycolate lyase. Involved in the final step of biosynthesis of alpha-melanotropin and related biologically active peptides.
SYNONYMS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PAM
-
-
-
-
PAM-A
-
-
-
-
PAM-B
-
-
-
-
peptide alpha-amidating enzyme
-
-
-
-
peptide alpha-amide synthase
-
-
-
-
peptide-alpha-amide synthetase
-
-
-
-
peptidyl alpha-amidating enzyme
-
-
-
-
peptidylglycine 2-hydroxylase
-
-
-
-
peptidylglycine alpha-amidating monooxygenase
-
-
-
-
peptidylglycine alpha-hydroxylase
-
-
-
-
synthase, peptide alpha-amide
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
90597-47-0
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
2 forms: a soluble and a membrane-bound; marine mollusc
-
-
Manually annotated by BRENDA team
2 forms: A and B
-
-
Manually annotated by BRENDA team
Frog
-
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
bifunctional enzyme
-
-
Manually annotated by BRENDA team
bifunctional enzyme showing peptidylglycine alpha-hydroxylating monooxygenase, PHM, EC 1.14.17.3, and peptidylamidoglycolate lyase, PAL, EC 4.3.2.5, activities
SwissProt
Manually annotated by BRENDA team
ND4 Swiss Webster mice, suckling copper-deficient mice via copper-deficient diet
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
2 forms: type A and B
-
-
Manually annotated by BRENDA team
bifunctional copper- and zinc-dependent enzyme
-
-
Manually annotated by BRENDA team
bifunctional enzyme showing peptidylglycine alpha-hydroxylating monooxygenase, PHM, EC 1.14.17.3, and peptidylamidoglycolate lyase, PAL, EC 4.3.2.5, activities
-
-
Manually annotated by BRENDA team
Holtzman rats, copper-deficient rats via copper-deficient diet
-
-
Manually annotated by BRENDA team
PAM-1 and PAM-2
-
-
Manually annotated by BRENDA team
Sprague-Dawley, at least 3 different splicing variants PAM-1, PAM-2, and PAM-3
-
-
Manually annotated by BRENDA team
3 genetic forms, 2 protein forms of amidating enzyme: protein form 1, gene AE-I, has only peptidylglycine alpha-hydroxylating activity, protein form 2, genes AE-III and AE-II, show peptidylglycine alpha-hydroxylating activity and peptidylhydroxylglycine N-C lyase activity
-
-
Manually annotated by BRENDA team
peptidylglycine alpha-hydroxylating monooxygenase activity
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
copper metabolism is altered by PAM
physiological function
-
regulation of the hypothalamic-pituitary-thyroid axis and body temperature are selected for evaluation
physiological function
-
essential for the synthesis of all amidated neuropeptides, mice lacking peptidylglycine alpha-amidating monooxygenase do not survive gestation
physiological function
P19021
most mammalian bioactive peptides possess a C-terminal amino acid amide moiety. Amidated peptides are produced in vivo by the enzymatic cleavage of a precursor with a C-terminal glycine residue. The enzyme catalyzes the key step in the oxidation of the glycine-extended precursors to the alpha-amidated peptide
physiological function
-
the enzyme is a regulator of copper homeostasis in neuroendocrine cells
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(([(1E)-phenylmethylidene]amino)oxy)acetic acid + ascorbate + O2
(2R)-hydroxy(([(1E)-phenylmethylidene]amino)oxy)ethanoic acid + ?
show the reaction diagram
-
non-enzymatic dealkylation yields benzaldoxime and glyoxylate
-
-
?
2,6-difluorohippuric acid + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
2-aminohippuric acid + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
2-hydroxyhippuric acid + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
2-iodohippuric acid + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
2-methylhippuric acid + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
2-propylmercaptoacetylglycine + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
2-pyridylmercaptoacetylglycine + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
3-(2-furyl)acryloylglycine + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
3-chlorohippuric acid + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
3-indolylacetylglycine + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
3-methylhippuric acid + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
3-phenylthiopropionylglycine + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
4-aminohippuric acid + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
4-bromohippuric acid + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
4-chlorohippuric acid + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
4-dimethylaminoazobenzene-4'-sulfonyl-Gly-L-Phe-Gly + ascorbate + O2
4-dimethylaminoazobenzene-4'-sulfonyl-Gly-L-Phe-2-hydroxyglycine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
4-ethylhippuric acid + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
4-hydroxyhippuric acid + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
4-methoxyhippuric acid + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
4-methylhippuric acid + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
4-nitrobenzoyl-Gly-Gly + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
4-nitrohippuric acid + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
4-phenylbutyrylglycine + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
4-propylhippuric acid + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
4-trifluoromethylhippuric acid + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
5-phenylpentanoylglycine + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
6-phenylhexanoylglycine + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
8-phenyloctanoylglycine + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
acetyl-D-alanine + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
acetyl-Gly-Gly + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
acetyl-L-Tyr-L-Val-Gly + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
adrenocorticotrophic hormone(9-14) + ascorbate + O2
adrenocorticotrophic hormone(9-13)-2-hydroxyglycine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
Ala-Ile-Gly-Val-Gly-Ala-Pro-Gly + ascorbate + O2
Ala-Ile-Gly-Val-Gly-Ala-Pro-2-hydroxyglycine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
Ala-Ile-Gly-Val-Gly-Ala-Pro-Gly + ascorbate + O2
Ala-Ile-Gly-Val-Gly-Ala-Pro-2-hydroxyglycine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
alanyl-L-phenylalanylglycine + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
alanyl-L-prolylglycine + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
alanylglycyl-L-phenylalanylglycine + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
alanylglycyl-L-prolylglycine + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
alanylglycylvalyl-L-phenylalanylglycine + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
alanylglycylvalyl-L-prolylglycine + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
alpha-N-acetyl-adrenocorticotrophic hormone(1-14) + ascorbate + O2
alpha-N-acetyl-adrenocorticotrophic hormone(1-13)-2-hydroxyglycine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
alpha-N-acetyl-adrenocorticotrophic hormone(1-14) + ascorbate + O2
alpha-N-acetyl-adrenocorticotrophic hormone(1-13)-2-hydroxyglycine + dehydroascorbate + H2O
show the reaction diagram
-
inhibitory substrate
-
r
alpha-N-acetyl-Tyr-Val-Gly + ascorbate + O2
alpha-N-acetyl-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
alpha-N-acetyl-Tyr-Val-Gly + ascorbate + O2
alpha-N-acetyl-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
alpha-N-acetyl-Tyr-Val-Gly + ascorbate + O2
alpha-N-acetyl-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
alpha-N-acetyl-Tyr-Val-Gly + ascorbate + O2
alpha-N-acetyl-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
alpha-N-acetyl-Tyr-Val-Gly + ascorbate + O2
alpha-N-acetyl-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
benzaldehyde imino-oxy acetic acid + O2
benzaldoxime + glyoxylate
show the reaction diagram
-
assay at 37C, pH 6.0
-
-
?
benzoyl-D-alanine + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
CBZ-D-alanine + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
CBZ-glycine + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
chloroacetyl-Gly-Gly + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
cinnamoylglycine + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
D-iodo-Tyr-Val-Gly + ascorbate + O2
D-iodo-Tyr-Val-(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
P19021
labeled substrate
the carbinol is the substrate for the peptidylamidoglycolate lyase reaction, EC 4.3.2.5, forming glyoxylate and amidated peptide
-
?
D-Tyr-Pro-Gly-Gly + ascorbate + O2
D-Tyr-Pro-Gly-2-hydroxyglycine + dehydroascorbate + H2O
show the reaction diagram
-
synthetic peptide, optimal activity in sulfonic acid buffers
-
?
D-Tyr-Val-Gly + ascorbate + O2
D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
D-Tyr-Val-Gly + ascorbate + O2
D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
D-Tyr-Val-Gly + ascorbate + O2
D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
D-Tyr-Val-Gly + ascorbate + O2
D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
D-Tyr-Val-Gly + ascorbate + O2
D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
D-Tyr-Val-Gly + ascorbate + O2
D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
D-Tyr-Val-Gly + ascorbate + O2
D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
D-Tyr-Val-Gly + ascorbate + O2
D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
D-Tyr-Val-Gly + ascorbate + O2
D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
D-Tyr-Val-Gly + ascorbate + O2
D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
D-Tyr-Val-Gly + ascorbate + O2
D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
show the reaction diagram
-
synthetic peptid
-
?
D-Tyr-Val-Gly + ascorbate + O2
D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
show the reaction diagram
-
synthetic peptid
-
?
D-Tyr-Val-Gly + ascorbate + O2
D-Tyr-Val-NH2 + glyoxylate + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
D-Tyr-Val-Gly + ascorbate + O2
D-Tyr-Val-NH2 + glyoxylate + dehydroascorbate + H2O
show the reaction diagram
Frog
-
synthetic substrate
-
-
?
dansyl-D-Tyr-Val-Gly + ascorbate + O2
dansyl-D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
dansyl-D-Tyr-Val-Gly + ascorbate + O2
dansyl-D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
dansyl-D-Tyr-Val-Gly + ascorbate + O2
dansyl-D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
dansyl-D-Tyr-Val-Gly + ascorbate + O2
dansyl-D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
show the reaction diagram
-
stereospecific
-
-
?
dansyl-D-Tyr-Val-Gly + H2O2
dansyl-D-Tyr-Val-2-hydroxyglycine + H2O
show the reaction diagram
-
peptidylglycine monooxygenase is able to catalyze the hydroxylation of peptidylglycine substrates starting from the oxidized enzyme and using hydrogen peroxide as the only source of oxygen
-
-
?
dansyl-Gly-Gly-Ser-CO-NH-CH2-COOH + ascorbate + O2
?
show the reaction diagram
-
substrate contains either protium or deuterium at the CH2-group
-
-
?
dansyl-L-Tyr-L-Val-Gly + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
dansyl-L-Tyr-L-Val-Gly + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
dansyl-YVG + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
dansyl-YVG-COOH + ascorbate + O2
dansyl-YV-NH2 + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
gamma-Glu-Gly-Gly + ascorbate + O2
gamma-Glu-Gly-NH2 + glyoxylate + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
glutathione + ascorbate + O2
gamma-Glu-Cys-NH2 + glyoxylate + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
glyoxylic acid phenylhydrazone + ascorbate + O2
oxalate phenylhydrazide + dehydroascorbate + H2O
show the reaction diagram
-
competitive substrate, inhibitory
-
?
hippuric acid + ascorbate + O2
alpha-hydroxyhippuric acid + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
-
hippuric acid + ascorbate + O2
alpha-hydroxyhippuric acid + dehydroascorbate + H2O
show the reaction diagram
-
i.e. N-benzoylglycine
-
?
hippuric acid + ascorbate + O2
alpha-hydroxyhippuric acid + dehydroascorbate + H2O
show the reaction diagram
-
i.e. N-benzoylglycine
-
?
hippuric acid + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
Frog
-
synthetic substrate
-
-
ir
hippuric acid + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
C-H bond cleavage is irreversible, protiated and dideuterated substrate
-
-
ir
hippuric acid + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
hippuric acid + ferrocyanide + O2
alpha-hydroxyhippuric acid + ? + H2O
show the reaction diagram
-
-
-
-
-
hippuryl-Gly + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
hippuryl-Gly-Gly + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
HOOC-NH-CH2-COOH + ascorbate + O2
?
show the reaction diagram
-
substrate contains either protium or deuterium at the CH2-group
-
-
?
hydrocinnamoylglycine + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
isocaproylglycine + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
L-phenylalanylglycine + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
L-prolylglycine + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
L-pyroglutamyl-Gly + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
leukotriene C4 + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
monoiodo-alpha-N-acetyl-Tyr-Val-Gly + ascorbate + O2
monoiodo-alpha-N-acetyl-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
monoiodo-alpha-N-acetyl-Tyr-Val-Gly + ascorbate + O2
monoiodo-alpha-N-acetyl-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
monoiodo-alpha-N-acetyl-Tyr-Val-Gly + ascorbate + O2
monoiodo-alpha-N-acetyl-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
N-(2,4,6-trinitrophenyl)-D-Tyr-Val-Gly + ascorbate + O2
N-(2,4,6-trinitrophenyl)-D-Tyr-Val-(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
N-(2-furoyl)glycine + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
N-(2-thienylcarbonyl)glycine + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
N-(4-amino-6-methyl-3-oxoheptanoyl)-L-phenylalanylglycine + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
N-(4-amino-6-methyl-3-oxoheptanoyl)glycylglycine + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
N-(4-nitrobenzyl)glycine + ascorbate + O2
nitrobenzylamine + glyoxylate + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
N-(alpha-methylhydrocinnamoyl)glycine + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
N-(phenylacetyl)glycine + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
N-(phenylacetyl)glycine + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
N-acetyl-Arg-Gly-Gly + ascorbate + O2
N-acetyl-Arg-Gly-hydroxyglycin + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
-
N-acetyl-Gln-Lys-Glu-Ser-Thr-Leu-His-Leu-Val-Leu-Arg-Leu-Arg-Gly-Gly + ascorbate + O2
N-acetyl-Leu-Arg-Gly-hydroxyglycin + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
-
N-acetyl-L-Phe-Gly + ascorbate + O2
N-acetyl-L-Phe-2-hydroxyglycine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
N-acetyl-L-phenylalanylglycine + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
N-acetyl-Leu-Arg-Gly-Gly + ascorbate + O2
N-acetyl-Leu-Arg-Gly-hydroxyglycin + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
-
N-acetyl-Leu-Arg-Leu-Arg-Gly-Gly + ascorbate + O2
N-acetyl-Leu-Arg-Gly-hydroxyglycin + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
-
N-acetyl-Leu-His-Leu-Val-Leu-Arg-Leu-Arg-Gly-Gly + ascorbate + O2
N-acetyl-Leu-Arg-Gly-hydroxyglycin + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
-
N-acetyl-Tyr-Val-Gly + ascorbate + O2
N-acetyl-Tyr-Val-(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
N-acetylglycine + 2 ascorbate + O2
N-acetyl-2-hydroxyglycine + 2 semidehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
N-acetylglycine + ascorbate + O2
acetylamine + glyoxylate + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
N-acetylglycine + ascorbate + O2
N-acetyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
N-acetylglycine + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
N-acetylglycine + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
N-acetylglycylglycine + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
N-benzoylglycine + ascorbate + O2
N-benzoyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
N-butyrylglycine + 2 ascorbate + O2
N-butyryl-2-hydroxyglycine + 2 semidehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
N-Dan-Tyr-Val-Gly + ascorbate + O2
N-Dan-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
show the reaction diagram
-
PAM activity assay, the product is unstable and dismutates to N-Dan-Tyr-Val-NH2 and glyoxylate (EC4.3.2.5)
-
-
?
N-Dan-Tyr-Val-Gly + ascorbate + O2
N-Dan-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
show the reaction diagram
-
the product is unstable and dismutates to N-Dan-Tyr-Val-NH2 and glyoxylate (EC4.3.2.5)
-
-
?
N-DANSYL-D-Tyr-L-Val-Gly + ascorbate + O2
N-DANSYL-D-Tyr-L-Val-(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
N-dansyl-Tyr-Val-D-Ala + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
N-dansyl-Tyr-Val-Gly + ascorbate + O2
N-dansyl-Tyr-Val-(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
P19021
-
-
-
?
N-decanoylglycine + 2 ascorbate + O2
N-decanoyl-2-hydroxyglycine + 2 semidehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
N-decanoylglycine + ascorbate + O2
decanoylamine + glyoxylate + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
N-decanoylglycine + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
N-hexanoylglycine + 2 ascorbate + O2
N-hexanoyl-2-hydroxyglycine + 2 semidehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
N-hexanoylglycine + ascorbate + O2
hexanoylamine + glyoxylate + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
N-octanoylglycine + 2 ascorbate + O2
N-octanoyl-2-hydroxyglycine + 2 semidehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
N-propionylglycine + 2 ascorbate + O2
N-propionyl-2-hydroxyglycine + 2 semidehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
N-trifluoroacetylglycine + ascorbate + O2
N-trifluoroacetyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
N-trinitrophenyl-D-Tyr-Val-Gly + ascorbate + O2
N-trinitrophenyl-D-Tyr-Val-(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
the carbinol is the substrate for the peptidylamidoglycolate lyase reaction, EC 4.3.2.5, forming glyoxylate and amidated peptide
-
?
N-trinitrophenyl-D-Tyr-Val-Gly + ascorbate + O2
N-trinitrophenyl-D-Tyr-Val-(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
P19021
-
the carbinol is the substrate for the peptidylamidoglycolate lyase reaction, EC 4.3.2.5, forming glyoxylate and amidated peptide
-
?
N-trinitrophenyl-D-Tyr-Val-Gly + ascorbate + O2
N-trinitrophenyl-D-Tyr-Val-NH2 + glyoxylate + dehydroascorbate + H2O
show the reaction diagram
Frog
-
synthetic substrate
-
-
?
N-[(benzylmercapto)carbonyl]glycine + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
N-[(phenylcyclopropyl)carbonyl]glycine + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
N-[3-(1-leucylpyrrolidin-2-yl)-3-oxopropanoyl]-L-phenylalanylglycine + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
N-[3-(1-leucylpyrrolidin-2-yl)-3-oxopropanoyl]glycylglycine + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
nicotinuric acid + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
O-acetyl-L-mandelyl-Gly + ascorbate + O2
O-acetyl-L-mandelyl-2-hydroxyglycine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
peptidyl-glycine + ascorbate + O2
peptidyl-(2-hydroxylglycine) + dehydroascorbate + H2O
show the reaction diagram
-
PHM catalyzes the stereospecific hydroxylation of the glycine alpha-carbon of all peptidylglycine substrates
-
-
?
peptidylglycine + 2 ascorbate + O2
peptidyl(2-hydroxyglycine) + 2 semidehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
requirement for O2
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
requirement for O2
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
requirement for O2
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
requirement for O2
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
requirement for O2
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
requirement for O2
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
requirement for O2
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
diverse synthetic substrates with C-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
COOH-terminal glycine
semidehydroascorbate
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
amidation of neurohormonal peptides
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
peptidylglycine alpha-hydroxylating monooxygenase reaction
the carbinol is the substrate for the peptidylamidoglycolate lyase reaction, EC 4.3.2.5, forming glyoxylate and amidated peptide
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
peptidylglycine alpha-hydroxylating monooxygenase reaction
the carbinol is the substrate for the peptidylamidoglycolate lyase reaction, EC 4.3.2.5, forming glyoxylate and amidated peptide
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
P19021
peptidylglycine alpha-hydroxylating monooxygenase reaction
the carbinol is the substrate for the peptidylamidoglycolate lyase reaction, EC 4.3.2.5, forming glyoxylate and amidated peptide
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
2 Cu2+, A and B, are involved in the catalytic reaction
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
C-H bond cleavage is irreversible, activation of molecular O2 and of the C-H bond of the substrate, mechanism, reductive activation of Cu(II)-OOH to generate a reactive copper-oxo species
-
-
ir
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
formation of a CuIIM-OOH intermediate, intramolecular electron transfer
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
Q4W7B5
peptidylglycine alpha-hydroxylating monooxygenase PHM reaction
the carbinol is the substrate for the peptidylamidoglycolate lyase reaction, EC 4.3.2.5, forming glyoxylate and amidated peptide
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
peptidylglycine alpha-hydroxylating monooxygenase reaction, diverse glycine derivatives or substitutes
the carbinol is the substrate for the peptidylamidoglycolate lyase reaction, EC 4.3.2.5, forming glyoxylate and amidated peptide
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
P19021
most mammalian bioactive peptides possess a C-terminal amino acid amide moiety. Amidated peptides are produced in vivo by the enzymatic cleavage of a precursor with a C-terminal glycine residue. The enzyme catalyzes the key step in the oxidation of the glycine-extended precursors to the alpha-amidated peptide
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxylglycine) + dehydroascorbate + H2O
show the reaction diagram
-
peptidylglycine alpha-hydroxylating monooxygenase reaction
the carbinol is the substrate for the peptidylamidoglycolate lyase reaction, EC 4.3.2.5, forming glyoxylate and amidated peptide
-
?
peptidylglycine + ascorbate + O2
peptidyl (S)-2-hydroxyglycine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl alpha-hydroxyglycine + semidehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl alpha-hydroxyglycine + semidehydroascorbate + H2O
show the reaction diagram
J9QK52, J9QL63
-
-
-
?
Phe-Gly-Phe-Gly + ascorbate + O2
Phe-Gly-Phe-2-hydroxyglycine + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
Phe-Gly-Phe-Gly + ascorbate + O2
Phe-Gly-Phe-(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
phenylhydantoic acid + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
phenylmercaptoacetylglycine + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
phenylthioacetylglycine + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
R-CO-NH-CH2-COOH + ascorbate + O2
R-CO-NH2 + CHO-COOH + dehydroascorbate + H2O
show the reaction diagram
-
via hydroxylated reaction intermediates
-
-
?
S-(1,2-dicarboxyethyl)-glutathione + ascorbate + O2
S-(1,2-dicarboxyethyl)-gamma-Glu-Cys-NH2 + glyoxylate + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
S-(4-nitrobenzyl)-glutathione + ascorbate + O2
S-(4-nitrobenzyl)-gamma-Glu-Cys-NH2 + glyoxylate + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
S-butyl-glutathione + ascorbate + O2
S-butyl-gamma-Glu-Cys-NH2 + glyoxylate + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
S-decyl-glutathione + ascorbate + O2
S-decyl-gamma-Glu-Cys-NH2 + glyoxylate + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
S-ethyl-glutathione + ascorbate + O2
S-ethyl-gamma-Glu-Cys-NH2 + glyoxylate + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
S-hexyl-glutathione + ascorbate + O2
S-hexyl-gamma-Glu-Cys-NH2 + glyoxylate + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
S-methyl-glutathione + ascorbate + O2
S-methyl-gamma-Glu-Cys-NH2 + glyoxylate + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
S-octyl-glutathione + ascorbate + O2
S-octyl-gamma-Glu-Cys-NH2 + glyoxylate + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
S-propyl-glutathione + ascorbate + O2
S-propyl-gamma-Glu-Cys-NH2 + glyoxylate + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
tBOC-Gly + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
tBOC-Gly-Gly + ascorbate + O2
?
show the reaction diagram
-
-
-
-
?
trinitrophenyl-D-Tyr-Val-Gly + ascorbate + O2
trinitrophenyl-D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
show the reaction diagram
-
COOH-terminal glycine
-
-
?
trinitrophenyl-D-Tyr-Val-Gly + ascorbate + O2
?
show the reaction diagram
-
activity assay
-
-
?
ubiquitin + ascorbate + O2
? + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
-
[(4-nitrobenzyl)oxy]acetic acid + ascorbate + O2
nitrobenzyl alcohol + glyoxylate + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
monoiodo-D-Tyr-Val-Gly + ascorbate + O2
monoiodo-D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
show the reaction diagram
-
synthetic peptid
-
?
additional information
?
-
-
specificity
-
-
-
additional information
?
-
-
substrate specificity
-
-
-
additional information
?
-
-
at alkaline pH spontaneous conversion
-
-
-
additional information
?
-
-
cleavage of C-H bond in the second reaction step is irreversible
-
-
-
additional information
?
-
-
endorphins are inhibitory substrates
-
-
-
additional information
?
-
-
EC 1.14.17.3 is often called peptidylglycine alpha-amidating monooxygenase (PAM) and the alpha-amidated product is mentioned as the product of the reaction, but the alpha-amidation of glycine-extended peptides is a two-step process catalyzed by 2 enzymes: 1. EC 1.14.17.3: production of peptidyl(2-hydroxyglycine) by a copper, molecular oxygen and ascorbate-dependent peptidyl-glycine alpha-hydroxylating monooxygenase (PMH) and 2. conversion of the peptidyl-alpha-hydroxyglycine derivative into an alpha-amidated product at physiological pH by peptidyl-alpha-hydroxyglycine alpha-amidating lyase
-
-
-
additional information
?
-
-
EC 1.14.17.3 is often called peptidylglycine alpha-amidating monooxygenase (PAM) and the alpha-amidated product is mentioned as the product of the reaction, but the alpha-amidation of glycine-extended peptides is a two-step process catalyzed by 2 enzymes: 1. EC 1.14.17.3: production of peptidyl(2-hydroxyglycine) by a copper, molecular oxygen and ascorbate-dependent peptidyl-glycine alpha-hydroxylating monooxygenase (PMH) and 2. conversion of the peptidyl-alpha-hydroxyglycine derivative into an alpha-amidated product at physiological pH by peptidyl-alpha-hydroxyglycine alpha-amidating lyase
-
-
-
additional information
?
-
-
EC 1.14.17.3 is often called peptidylglycine alpha-amidating monooxygenase (PAM) and the alpha-amidated product is mentioned as the product of the reaction, but the alpha-amidation of glycine-extended peptides is a two-step process catalyzed by 2 enzymes: 1. EC 1.14.17.3: production of peptidyl(2-hydroxyglycine) by a copper, molecular oxygen and ascorbate-dependent peptidyl-glycine alpha-hydroxylating monooxygenase (PMH) and 2. conversion of the peptidyl-alpha-hydroxyglycine derivative into an alpha-amidated product at physiological pH by peptidyl-alpha-hydroxyglycine alpha-amidating lyase
-
-
-
additional information
?
-
-
EC 1.14.17.3 is often called peptidylglycine alpha-amidating monooxygenase (PAM) and the alpha-amidated product is mentioned as the product of the reaction, but the alpha-amidation of glycine-extended peptides is a two-step process catalyzed by 2 enzymes: 1. EC 1.14.17.3: production of peptidyl(2-hydroxyglycine) by a copper, molecular oxygen and ascorbate-dependent peptidyl-glycine alpha-hydroxylating monooxygenase (PMH) and 2. conversion of the peptidyl-alpha-hydroxyglycine derivative into an alpha-amidated product at physiological pH by peptidyl-alpha-hydroxyglycine alpha-amidating lyase
-
-
-
additional information
?
-
-
substrates are also physiologically relevant peptides related to alpha-melanotropine
-
-
-
additional information
?
-
-
substrates are also physiologically relevant peptides related to alpha-melanotropine
-
-
-
additional information
?
-
-
acetyl-L-Phe-Gly, acetyl-L-Phe-L-Phe-Gly, or (S)-O-acetyl-mandelyl-Gly, and stereoisomers are alpha-hydroxylated but not alpha-amidated
-
-
-
additional information
?
-
-
tunneling of hydrogen ion, relatively flexible
-
-
-
additional information
?
-
-
PAM catalyzes: 1. sulfoxidation of e.g. (4-nitrobenzyl) thioacetic acid to the analogous sulfoxide, 2. amine N-dealkylation of e.g. N-(4-nitrobenzyl)glycine to 4-nitrobenzylamine and glyoxylate, 3. O-dealkylation of e.g. [(4-nitrobenzyl)oxy]acetic acid to 4-nitrobenzyl alcohol and glyoxylate, 4. transformation of hippuric acid and several ring-substituted derivatives to the corresponding benzoamides and glyoxylic acid
-
-
-
additional information
?
-
-
cleavage of CN bond in N-acetylated glycines, R-CO-NH-CH2-COOH, e.g. found in neuropeptide prohormones, inhibition of the enzyme leads to a decrease in alpha-aminated peptide production and accumulation of glycine-extended precursors
-
-
-
additional information
?
-
-
enzyme catalyzes the biosynthesis of peptide hormones through radical cleavage of the C-terminal glycine residues of the corresponding prohormones
-
-
-
additional information
?
-
-
enzyme catalyzes the production of neurohormones and neurotransmitters
-
-
-
additional information
?
-
-
enzyme is involved in peptide posttranslational activation
-
-
-
additional information
?
-
-
enzyme is required for amidation of autocrine growth factors causing proliferation in tumor cells
-
-
-
additional information
?
-
-
enzyme is required for amidation of autocrine growth factors causing proliferation in tumor cells
-
-
-
additional information
?
-
Q4W7B5
enzyme is required for amidation of the C-terminus of neuropeptides
-
-
-
additional information
?
-
-
enzyme might be involved in secretory vesicle budding and fusion in the cardiac ANP-secretory pathway
-
-
-
additional information
?
-
Frog
-
peptide alpha-amidation, enzyme is responsible for formation of peptide C-terminal amide, peptide alpha-amidation, the N-terminal substrate structure affects the interaction with the active site of the enzyme
-
-
-
additional information
?
-
-
substrate specificity, cleavage of CN bond in N-acetylated glycines, R-CO-NH-CH2-COOH, e.g. found in neuropeptide prohormones
-
-
-
additional information
?
-
-
substrate specificity, effects of substitutions on the glycine substrate, overview
-
-
-
additional information
?
-
-
long distance electron-transfer mechanism between the two distant copper cations, a perfect fitting for a water bridge, molecular dynamics simulations using wild-type and mutant enzymes, overview
-
-
-
additional information
?
-
-
PAM is the only enzyme capable of amidating peptides, amidated peptides are numerous
-
-
-
additional information
?
-
-
PAM is the rate-limiting enzyme for the generation of carboxy-terminal alpha-amidated neuropeptides
-
-
-
additional information
?
-
-
PHM replaces the pro-(S) hydrogen of the carboxy-terminal glycine with a hydroxyl group to form an alpha-hydroxyglycine intermediate
-
-
-
additional information
?
-
-
PAM carries out two functions, peptidyl alpha-hydroxylating monooxygenase and peptidylamido-glycolate lyase activities
-
-
-
additional information
?
-
-
the enzyme peptidylglycine alpha-amidating monooxygenase consists of two subunits: peptidylglycine alpha-hydroxylating monooxygenase that initiates formation of a radical at a substrate's C-terminal glycine alpha-carbon to then give an alpha-hydroxylated glycine derivative, and peptidylamidoglycolate lyase which catalyzes cleavage of this hydroxyglycine intermediate to give the amidated product with consequent release of glyoxylate
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
peptidyl-glycine + ascorbate + O2
peptidyl-(2-hydroxylglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
COOH-terminal glycine
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
amidation of neurohormonal peptides
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
peptidylglycine alpha-hydroxylating monooxygenase reaction
the carbinol is the substrate for the peptidylamidoglycolate lyase reaction, EC 4.3.2.5, forming glyoxylate and amidated peptide
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
-
peptidylglycine alpha-hydroxylating monooxygenase reaction
the carbinol is the substrate for the peptidylamidoglycolate lyase reaction, EC 4.3.2.5, forming glyoxylate and amidated peptide
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
show the reaction diagram
P19021
most mammalian bioactive peptides possess a C-terminal amino acid amide moiety. Amidated peptides are produced in vivo by the enzymatic cleavage of a precursor with a C-terminal glycine residue. The enzyme catalyzes the key step in the oxidation of the glycine-extended precursors to the alpha-amidated peptide
-
-
?
peptidylglycine + ascorbate + O2
peptidyl(2-hydroxylglycine) + dehydroascorbate + H2O
show the reaction diagram
-
peptidylglycine alpha-hydroxylating monooxygenase reaction
the carbinol is the substrate for the peptidylamidoglycolate lyase reaction, EC 4.3.2.5, forming glyoxylate and amidated peptide
-
?
peptidylglycine + ascorbate + O2
peptidyl alpha-hydroxyglycine + semidehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
peptidylglycine + ascorbate + O2
peptidyl alpha-hydroxyglycine + semidehydroascorbate + H2O
show the reaction diagram
J9QK52, J9QL63
-
-
-
?
R-CO-NH-CH2-COOH + ascorbate + O2
R-CO-NH2 + CHO-COOH + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
glutathione + ascorbate + O2
gamma-Glu-Cys-NH2 + glyoxylate + dehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
cleavage of CN bond in N-acetylated glycines, R-CO-NH-CH2-COOH, e.g. found in neuropeptide prohormones, inhibition of the enzyme leads to a decrease in alpha-aminated peptide production and accumulation of glycine-extended precursors
-
-
-
additional information
?
-
-
enzyme catalyzes the biosynthesis of peptide hormones through radical cleavage of the C-terminal glycine residues of the corresponding prohormones
-
-
-
additional information
?
-
-
enzyme catalyzes the production of neurohormones and neurotransmitters
-
-
-
additional information
?
-
-
enzyme is involved in peptide posttranslational activation
-
-
-
additional information
?
-
-
enzyme is required for amidation of autocrine growth factors causing proliferation in tumor cells
-
-
-
additional information
?
-
-
enzyme is required for amidation of autocrine growth factors causing proliferation in tumor cells
-
-
-
additional information
?
-
Q4W7B5
enzyme is required for amidation of the C-terminus of neuropeptides
-
-
-
additional information
?
-
-
enzyme might be involved in secretory vesicle budding and fusion in the cardiac ANP-secretory pathway
-
-
-
additional information
?
-
Frog
-
peptide alpha-amidation, enzyme is responsible for formation of peptide C-terminal amide
-
-
-
additional information
?
-
-
PAM is the only enzyme capable of amidating peptides, amidated peptides are numerous
-
-
-
additional information
?
-
-
PAM is the rate-limiting enzyme for the generation of carboxy-terminal alpha-amidated neuropeptides
-
-
-
additional information
?
-
-
PHM replaces the pro-(S) hydrogen of the carboxy-terminal glycine with a hydroxyl group to form an alpha-hydroxyglycine intermediate
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ascorbate
-
dependent on
ascorbate
-
dependent on
ascorbate
-
dependent on
ascorbate
-
dependent on
ascorbate
-
dependent on
ascorbate
Q4W7B5
-
ascorbate
Frog
-
-
ascorbate
-
-
ascorbate
J9QK52, J9QL63
dependent on; dependent on
FAD
-
slight activity with
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
P19021
3.26 mol per mol of bifunctional enzyme
copper
-
dependent on, copper-deficiency decreases the enzyme activity, tissue copper status, overview
copper
Q4W7B5
essentially required for activity, 2 atoms bound by 5 conserved His residues and 1 conserved Met residue
copper
-
inter-copper electron transfer, mechanism, structure, 2 copper atoms per enzyme
copper
-
metalloenzyme, required for catalysis, bound at the active site
copper
-
-
copper
-
the enzyme contains two mononuclear Cu centers
copper
-
a cuproenzyme
copper
J9QK52, J9QL63
required for activity; required for activity
Cu2+
-
a copper protein; Cu2+ is absolutely required for optimal activity
Cu2+
-
a copper protein; Cu2+ strongly stimulates activity
Cu2+
-
a copper protein; Cu2+ is absolutely required for optimal activity
Cu2+
-
Cu2+ strongly stimulates activity
Cu2+
-
a copper protein; Cu2+ is absolutely required for optimal activity
Cu2+
-
Cu2+ is absolutely required for optimal activity
Cu2+
-
-
Cu2+
-
Cu2+ is absolutely required for optimal activity; optimal activity at 0.016 mM
Cu2+
-
Cu2+ is absolutely required for optimal activity
Cu2+
-
2fold increase in activity
Cu2+
-
Cu2+ is absolutely required for optimal activity
Cu2+
-
Cu2+ to protein ration is 0.97
Cu2+
-
required for alpha-hydroxylation step
Cu2+
-
mutant H172A has reduced copper content: below 0.3 Cu2+ per protein molecule
Cu2+
P19021
required for peptidylglycine alpha-hydroxylating monooxygenase activity, 1.25 mol per mol of bifunctional enzyme
Cu2+
-
bifunctional copper- and zinc-dependent enzyme
Cu2+
-
required, reductive activation of Cu(II)-OOH to generate a reactive copper-oxo species
Cu2+
-
dependent on, metalloenzyme, binding analysis
Cu2+
-
required for peptidylglycine alpha-hydroxylating monooxygenase
Cu2+
-
oxygen activation by the noncoupled binuclear copper site, analysis of structure and electron transfer mechanism, formation of a CuIIM-OOH reaction intermediate, thermodynamics
Cu2+
-
-
Cu2+
-
The enzyme contains two copper centers, one performs the substrate hydroxylation, while the second is used for electron storage/transfer
Cu2+
-
requirred
Cu2+
-
a copper enzyme, copper binding ratios of recombinant catalytic core, overview
Cu2+
-
a noncoupled dicopper enzyme
Cu2+
-
required
Cu2+
-
peptidylglycine alpha-hydroxylating monooxygenase
Cu2+
-
-
Cu2+
-
required for activity
Fe2+
P19021
0.37 mol per mol of bifunctional enzyme
Mg2+
P19021
0.88 mol per mol of bifunctional enzyme
Zn2+
-
required for alpha-amidation step
Zn2+
P19021
required for peptidylamidoglycolate lyase activity, 0.62 mol per mol of bifunctional enzyme
Zn2+
-
bifunctional copper- and zinc-dependent enzyme
Zn2+
-
-
Zn2+
-
peptigylamidoglycolate lyase
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2E)-4-oxo-4-phenylbut-2-enoic acid
-
-
(3E)-4-(4-methoxyphenyl)but-3-enoic acid
-
-
(3E)-4-(4-methylphenyl)but-3-enoic acid
-
-
(3E)-4-[3-(benzyloxy)-4-methoxyphenyl]but-3-enoic acid
-
-
(3E)-4-[4-(benzyloxy)phenyl]but-3-enoic acid
-
-
(acetyloxy)acetic acid
-
-
(CBZ-hydrazido)glycine
-
-
(decanoylsulfanyl)acetic acid
-
-
(dodecanoyloxy)acetic acid
-
-
(nicotinamidomethyl)phosphonic acid
-
-
(R)-5-acetamido-4-oxo-6-phenyl-2-hexenoic acid
-
reversible and irreversible inhibition
(S)-5-acetamido-4-oxo-6-phenyl-2-hexenoic acid
-
reversible and irreversible inhibition
(S)-5-acetamido-7-methylthio-4-oxo-2-heptenoic acid
-
reversible and irreversible inhibition
(S)-N-CBZ-4-amino-2-hydroxybutyric acid
-
-
([(2S)-2-[(2-aminopropanoyl)amino]-3-phenylpropanoyl]oxy)acetic acid
-
-
([N-[3-(1-leucylpyrrolidin-2-yl)-3-oxopropanoyl]-L-phenylalanyl]oxy)acetic acid
-
-
([N-[3-(1-leucylpyrrolidin-2-yl)-3-oxopropanoyl]glycyl]oxy)acetic acid
-
-
([[(2S)-1-(2-aminopropanoyl)pyrrolidin-2-yl]carbonyl]oxy)acetic acid
-
-
([[(2S)-1-[[(2-aminopropanoyl)amino]acetyl]pyrrolidin-2-yl]carbonyl]oxy)acetic acid
-
-
([[(4-amino-6-methyl-3-oxoheptanoyl)amino]acetyl]oxy)acetic acid
-
-
3-benzoylpropionic acid
-
-
4-Phenyl-3-butenoic acid
-
mechanism-based inhibition
4-Phenyl-3-butenoic acid
-
binds to the lumenal side of the enzyme where the peptidylglycine alpha-hydroxylating PHM activity is localized
4-Phenyl-3-butenoic acid
-
irreversible turnover-dependent inhibition of the enzyme in vitro, at 0.1 mg/ml inhibition in vivo of proliferation of lung cancer cells and Ras-transformed WB rat liver epithelial cells, inhibitor leads to increased gap junction communication in the WB-Ras cells, overview
4-Phenyl-3-butenoic acid
-
-
4-Phenyl-3-butenoic acid
-
-
4-phenyl-3-butenoic acid methyl ester
-
at 0.01 mg/ml inhibition in vivo of proliferation of Ras-transformed WB rat liver epithelial cells, inhibitor leads to increased gap junction communication in the WB-Ras cells, overview
4-phenylbut-3-enoic acid
-
PBA
5-(acetylamino)-4-oxo-6-phenyl-2-hexenoic acid
-
-
5-(acetylamino)-4-oxo-6-phenyl-2-hexenoic acid methyl ester
-
-
6-O-palmitoyl-L-ascorbate
-
-
acetyl-D-Leu-OCH2COOH
-
-
acetyl-D-Phe-Gly
-
-
acetyl-D-Phe-OCH2COOH
-
-
acetyl-DL-Phe-OCH2COOH
-
-
acetyl-Gly-OCH2COOH
-
-
acetyl-L-Leu-OCH2COOH
-
-
acetyl-L-Phe-D-Phe-Gly
-
-
acetyl-L-Phe-Gly
-
only substrate for alpha-hydroxylation
acetyl-L-Phe-OCH2COOH
-
-
adrenocorticotrophic hormone(1-10)
-
-
alpha-N-acetyl-adrenocorticotrophic hormone(1-14)
-
-
ascorbate
-
above 0.4 mM for the purified enzyme, above 1.5 mM for the enzyme in crude extract
Cu2+
-
at higher concentration
D-Tyr-Pro-Gly-Gly
-
inhibition of activity with D-Tyr-Val-Gly
D-Tyr-Val-Gly
-
at 2 mM 82% inhibition, at 0.1 mM 45% inhibition
D-Tyr-Val-Gly
-
inhibition of activity with D-Tyr-Pro-Gly
D-Tyr-Val-Gly
-
inhibition above 20 mM of hydroxylation
decanoyloxyacetic acid
-
-
diethyldithiocarbamate
-
copper chelator
diethyldithiocarbamate
-
-
diethyldithiocarbamate
-
copper chelator
diethyldithiocarbamate
-
DDC
Disulfiram
-
-
dithiothreitol
-
-
EDTA
-
-
EDTA
-
recombinant enzyme, alpha-hydroxylation activity can be restored by Mn2+, Zn2+, Cd2+, and Co2+, but not by Ca2+, Cu2+, Mg2+, and Fe3+
endorphin(51-61)NH2
-
i.e. pro-adrenocorticotrophic hormone(1-10)
-
endorphins
-
and proendorphins
-
ferrocyanide
-
inhibiting above 0.6 mM
gamma-keto acid
-
-
-
glutathione ethyl ester
-
-
glycolate
-
-
Glyoxylate 2-pyridylhydrazone
-
-
Glyoxylate 4-carboxyphenylhydrazone
-
-
Glyoxylate benzylhydrazone
-
-
glyoxylate phenylhydrazone
-
strongly
Glyoxylate phenylsemicarbazone
-
-
Glyoxylate phenylthiosemicarbazone
-
-
Glyoxylate semicarbazone
-
-
glyoxylate thiosemicarbazone
-
-
glyoxylate-N-hexyl-4-carbamoylphenylhydrazone
-
strongly
hippuric acid
-
-
imidazole
-
-
N,S-dibenzoyl-L-cysteine
-
-
N-(benzoyl)-D-serine
-
-
N-(thiobenzoyl)-(D,L)-alanine
-
-
N-acetyl-D-Leu-OCH2COOH
-
competitive inhibitor
N-acetyl-D-Phe-Gly
-
-
N-acetyl-L-Leu-OCH2COOH
-
competitive inhibitor
N-acetyl-L-Phe-OCH2COOH
-
competitive inhibitor
N-benzylglycine
-
-
N-Carboxymethyl N'-phenylhydrazone
-
weak inhibition
N-phenylthiohydantoic acid
-
-
NaN3
-
-
O-(phenylcarbamoyl)glycolic acid
-
-
O-acetyl-D-mandelyl-Gly
-
-
O-benzamidoglycolic acid
-
-
p-hydroxymercuribenzoate
-
slightly
peptides
-
especially those with COOH-terminal glycine residues
phosphate
-
-
Pro-Leu-Gly hydroxamic acid
-
-
S-(2-phenylthioacetyl)thioglycolic acid
-
-
S-(3-phenylthiopropionyl)thioglycolic acid
-
-
S-(4-methylthiobenzoyl)thioglycolic acid
-
-
S-(4-methylthiobenzoyl)thioglycolic acid ethyl ester
-
-
S-(phenylthiocarbamoyl)-3-mercaptopropionic acid
-
-
S-(phenylthiocarbamoyl)thioglycolic acid
-
-
S-(thiobenzoyl)-(R,S)-thiolactic acid
-
-
S-(thiobenzoyl)-4-mercapto-4-cyanopentanoic acid
-
-
S-(thiobenzoyl)thioglycolic acid
-
-
S-(thiolauroyl)thioglycolic acid
-
-
S-phenylmercaptoacetic acid
-
-
Salicylhydroxamic acid
-
-
sulfite
-
irreversible inactivation is Cu2+-dependent
trans-Benzoylacrylic acid
-
mechanism-based inhibition
[(1R,2S)-2-phenylcyclopropyl]acetic acid
-
-
[(4-Methoxybenzoyl)oxy]acetic acid
-
-
[(phenylacetyl)oxy]acetic acid
-
-
[(phenylacetyl)sulfanyl]acetic acid
-
-
-
[[(2S)-2-(acetylamino)-3-phenylpropanoyl]oxy]acetic acid
-
-
[[(2S)-2-(acetylamino)-3-phenylpropanoyl]sulfanyl]acetic acid
-
-
[[(2S)-2-([[(2-aminopropanoyl)amino]acetyl]amino)-3-phenylpropanoyl]oxy]acetic acid
-
-
[[(2S)-2-amino-3-phenylpropanoyl]oxy]acetic acid
-
-
[[(2S)-pyrrolidin-2-ylcarbonyl]oxy]acetic acid
-
-
[[(acetylamino)acetyl]oxy]acetic acid
-
-
[[N-(4-amino-6-methyl-3-oxoheptanoyl)-L-phenylalanyl]oxy]acetic acid
-
-
Monoethyl fumarate
-
mechanism-based inhibition
additional information
-
activity is not affected by pepstatin A, phenylmethylsulfonyl fluoride, and soybean trypsin inhibitor
-
additional information
-
form 1, AE-I, competitive inhibition by tripeptides with C-terminal glycine, most effective is methione within these peptides
-
additional information
-
copper-deficiency decreases the enzyme activity
-
additional information
-
inhibition of peptidylglycine alpha-amidating monooxygenase by exploitation of factors affecting the stability and ease of formation of glycyl radicals, diverse glycine derivatives or substitutes, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
acetate
-
form 1, AE-I, activates below pH 6.0
chloride
-
form 1, AE-I, activates below pH 6.0
dexamethasone
-
increases gene expression 1.6fold, northern blot analysis
Iodide
-
form 1, AE-I, activates below pH 6.0
additional information
-
enzyme expression is induced by androgen-deprivation therapy
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
19
2,6-difluorohippuric acid
-
apparent KM
1.4
2-aminohippuric acid
-
apparent KM
0.86
2-hydroxyhippuric acid
-
apparent KM
3.4
2-iodohippuric acid
-
apparent KM
4.3
2-methylhippuric acid
-
apparent KM
0.22
2-propylmercaptoacetylglycine
-
apparent KM
0.036
2-pyridylmercaptoacetylglycine
-
apparent KM
1.2
3-(2-furyl)acryloylglycine
-
apparent KM
2.2
3-chlorohippuric acid
-
apparent KM
0.3
3-indolylacetylglycine
-
apparent KM
1.4
3-methylhippuric acid
-
apparent KM
0.038
3-phenylthiopropionylglycine
-
apparent KM
2.6
4-aminohippuric acid
-
apparent KM
0.52
4-bromohippuric acid
-
apparent KM
0.62
4-chlorohippuric acid
-
apparent KM
1.2
4-ethylhippuric acid
-
apparent KM
1.7
4-hydroxyhippuric acid
-
apparent KM
0.82
4-methoxyhippuric acid
-
apparent KM
1.8
4-methylhippuric acid
-
apparent KM
0.11
4-nitrobenzoyl-Gly-Gly
-
apparent KM
0.47
4-nitrohippuric acid
-
apparent KM
0.16
4-phenylbutyrylglycine
-
apparent KM
1.2
4-propylhippuric acid
-
apparent KM
0.77
4-trifluoromethylhippuric acid
-
apparent KM
0.15
5-phenylpentanoylglycine
-
apparent KM
0.051
6-phenylhexanoylglycine
-
apparent KM
0.1
8-phenyloctanoylglycine
-
apparent KM
1400
acetyl-D-alanine
-
apparent KM
1.5
acetyl-Gly-Gly
-
apparent KM
0.00035
acetyl-Tyr-Phe-Gly
-
in presence of 0.25 mM ascorbate
1.39
acetyl-Tyr-Phe-Gly
-
-
0.2
alanyl-L-phenylalanylglycine
-
pH and temperature not specified in the publication
4
alanyl-L-prolylglycine
-
pH and temperature not specified in the publication
0.035
alanylglycyl-L-phenylalanylglycine
-
pH and temperature not specified in the publication
3
alanylglycyl-L-prolylglycine
-
pH and temperature not specified in the publication
0.018
alanylglycylvalyl-L-phenylalanylglycine
-
pH and temperature not specified in the publication
0.96
alanylglycylvalyl-L-prolylglycine
-
pH and temperature not specified in the publication
0.292
alpha-hydroxyhippuric acid
-
0.4 mM ferrocyanide, 100 mM MES pH 6.0, 30 mM KCl, 1 microM CuSO4
84
benzoyl-D-alanine
-
apparent KM
35
CBZ-D-alanine
-
apparent KM
0.59
CBZ-glycine
-
apparent KM
0.42
chloroacetyl-Gly-Gly
-
apparent KM
0.23
cinnamoylglycine
-
apparent KM
0.033
D-Tyr-Pro-Gly-Gly
-
assayed without ascorbate and catalase, brain enzyme
0.068
D-Tyr-Pro-Gly-Gly
-
assayed without ascorbate and catalase, pituitary enzyme
0.075
D-Tyr-Pro-Gly-Gly
-
assayed with ascorbate and 0.1mg/ml catalase, pituitary enzyme
0.289
D-Tyr-Pro-Gly-Gly
-
assayed with ascorbate and 0.1 mg/ml catalase, brain enzyme
0.007
D-Tyr-Val-Gly
-
PAM-B, with 1.25 mM ascorbate
0.057
D-Tyr-Val-Gly
Frog
-
pH 7.5, 37C, recombinant enzyme
0.22
D-Tyr-Val-Gly
-
pH 6.0, 37C
0.022
dabsyl-Gly-Phe-Gly
-
form 2
0.143
dabsyl-Gly-Phe-Gly
-
form 1
0.00091
dansyl-D-Tyr-Val-Gly
-
at pH 7.0
0.003
dansyl-D-Tyr-Val-Gly
-
at pH 6.0
0.0051
dansyl-D-Tyr-Val-Gly
-
100 mM MES, pH 5.5, 0.2 mM dansyl-D-Tyr-Val-Gly, 5 microM CuSO4, ascorbate
0.0066
dansyl-D-Tyr-Val-Gly
-
at pH 5.0
0.0072
dansyl-D-Tyr-Val-Gly
-
at pH 5.5
0.8
dansyl-D-Tyr-Val-Gly
-
100 mM MES, pH 5.5, 0.2 mM dansyl-D-Tyr-Val-Gly, 5 microM CuSO4, 1 mM H2O2
0.0033
dansyl-L-Tyr-L-Val-Gly
-
mutant enzyme H107A, in100 mM MES pH 5.5, at 37C
-
0.0082
dansyl-L-Tyr-L-Val-Gly
-
wild type enzyme, in100 mM MES pH 5.5, at 37C
-
0.0118
dansyl-L-Tyr-L-Val-Gly
-
mutant enzyme M109I, in100 mM MES pH 5.5, at 37C
-
0.0194
dansyl-L-Tyr-L-Val-Gly
-
mutant enzyme H108A, in100 mM MES pH 5.5, at 37C
-
4.5
dansyl-Tyr-Phe-Gly
-
recombinant mutant AE-II, form 2
3.5
dansyl-Tyr-Phe-Gly(OH)
-
reaction product of step 1, substrate of step 2; recombinant mutant AE-II, form 2
0.003
dansyl-Tyr-Val-Gly
-
recombinant enzyme
0.03
ferrocyanide
-
4 mM alpha-hydroxyhippuric acid, 0.21 mM O2, 100 mM MES pH 6.0, 30 mM KCl, 1 microM CuSO4
0.26
ferrocyanide
-
40 mM alpha-hydroxyhippuric acid, 0.95 mM O2, 100 mM MES pH 6.0, 30 mM KCl, 1 microM CuSO4
2.1
gamma-Glu-Gly-Gly
-
pH 6.0, 37C
0.13
glutathione
-
pH 6.0, 37C
2.78
H2O2
-
100 mM MES, pH 5.5, 0.2 mM dansyl-D-Tyr-Val-Gly, 5 microM CuSO4, H2O2
0.61
hippuric acid
Frog
-
pH 5.0, 37C, recombinant enzyme
1.3
hippuric acid
-
apparent KM
0.078
hippuryl-Gly
-
apparent KM
0.31
hippuryl-Gly-Gly
-
apparent KM
0.94
hydrocinnamoylglycine
-
apparent KM
0.28
isocaproylglycine
-
apparent KM
0.28
L-ascorbate
-
+ 0.02 mM N-dansyl-Tyr-Phe-Gly
6.5
L-phenylalanylglycine
-
pH and temperature not specified in the publication
0.88
L-prolylglycine
-
pH and temperature not specified in the publication
0.31
L-pyroglutamyl-Gly
-
apparent KM
2.7
N-(2-furoyl)glycine
-
apparent KM
1.6
N-(2-thienylcarbonyl)glycine
-
apparent KM
0.011
N-(4-amino-6-methyl-3-oxoheptanoyl)-L-phenylalanylglycine
-
pH and temperature not specified in the publication
0.86
N-(4-amino-6-methyl-3-oxoheptanoyl)glycylglycine
-
pH and temperature not specified in the publication
4.1
N-(alpha-methylhydrocinnamoyl)glycine
-
apparent KM
0.16
N-(Phenylacetyl)glycine
-
apparent KM
0.33
N-(Phenylacetyl)glycine
-
pH and temperature not specified in the publication
0.12
N-acetyl-Arg-Gly-Gly
-
100 mM MES/NaOH, pH 6.0, 30 mM NaCl, 1% (v/v) ethanol, 0.001% (v/v) Triton X-100, 1 microM Cu(NO3)2, 10 mg/l catalase, 6 mM ascorbate, 8 microM N-dansyl-Tyr-Val-Gly
0.02
N-acetyl-Gln-Lys-Glu-Ser-Thr-Leu-His-Leu-Val-Leu-Arg-Leu-Arg-Gly-Gly
-
100 mM MES/NaOH, pH 6.0, 30 mM NaCl, 1% (v/v) ethanol, 0.001% (v/v) Triton X-100, 1 microM Cu(NO3)2, 10 mg/l catalase, 6 mM ascorbate, 8 microM N-dansyl-Tyr-Val-Gly
0.0079
N-acetyl-L-Phe-Gly
-
pH not specified in the publication, temperature not specified in the publication
0.015
N-acetyl-L-phenylalanylglycine
-
pH and temperature not specified in the publication
0.016
N-acetyl-L-phenylalanylglycine
-
pH and temperature not specified in the publication
0.13
N-acetyl-Leu-Arg-Gly-Gly
-
100 mM MES/NaOH, pH 6.0, 30 mM NaCl, 1% (v/v) ethanol, 0.001% (v/v) Triton X-100, 1 microM Cu(NO3)2, 10 mg/l catalase, 6 mM ascorbate, 8 microM N-dansyl-Tyr-Val-Gly
0.024
N-acetyl-Leu-Arg-Leu-Arg-Gly-Gly
-
100 mM MES/NaOH, pH 6.0, 30 mM NaCl, 1% (v/v) ethanol, 0.001% (v/v) Triton X-100, 1 microM Cu(NO3)2, 10 mg/l catalase, 6 mM ascorbate, 8 microM N-dansyl-Tyr-Val-Gly
0.018
N-acetyl-Leu-His-Leu-Val-Leu-Arg-Leu-Arg-Gly-Gly
-
100 mM MES/NaOH, pH 6.0, 30 mM NaCl, 1% (v/v) ethanol, 0.001% (v/v) Triton X-100, 1 microM Cu(NO3)2, 10 mg/l catalase, 6 mM ascorbate, 8 microM N-dansyl-Tyr-Val-Gly
0.0012
N-acetyl-Tyr-Val-Gly
-
purified recombinant wild-type enzyme, pH 7.0
0.0023
N-acetyl-Tyr-Val-Gly
-
purified recombinant mutant Y79W, pH 7.0
0.0029
N-acetyl-Tyr-Val-Gly
-
purified recombinant mutant Q170A, pH 7.0
0.0063
N-acetyl-Tyr-Val-Gly
-
purified recombinant wild-type enzyme, pH 5.5
0.0065
N-acetyl-Tyr-Val-Gly
-
purified recombinant mutant Q170A, pH 5.5
0.0098
N-acetyl-Tyr-Val-Gly
-
purified recombinant mutant Y79W, pH 5.5
9.3
N-acetylglycine
-
pH 6.0, 37C
9.3
N-acetylglycine
-
-
9.3
N-acetylglycine
-
apparent KM
9.9
N-acetylglycine
-
pH and temperature not specified in the publication
18
N-acetylglycine
-
pH 6.0, 37C
1.2
N-acetylglycylglycine
-
pH and temperature not specified in the publication
1.3
N-benzoylglycine
-
-
2.3
N-butyrylglycine
-
pH 6.0, 37C
0.0025
N-Dan-Tyr-Val-Gly
-
PHM activity in the soluble fraction of control and intermittent hypoxia brain stem ectracts
0.0032
N-dansyl-Tyr-Phe-Gly
-
+ 2 mM L-ascorbate
0.031
N-dansyl-Tyr-Val-D-Ala
-
apparent KM
0.0077
N-dansyl-Tyr-Val-Gly
P19021
pH 6.5, 37C
0.1
N-decanoylglycine
-
pH 6.0, 37C
0.11
N-decanoylglycine
-
pH 6.0, 37C
0.2
N-decanoylglycine
-
pH and temperature not specified in the publication
0.42
N-hexanoylglycine
-
pH 6.0, 37C
0.58
N-hexanoylglycine
-
pH 6.0, 37C
0.2
N-octanoylglycine
-
pH 6.0, 37C
2.4
N-propionylglycine
-
pH 6.0, 37C
4.1
N-trifluoroacetylglycine
-
-
0.0011
N-trinitrophenyl-D-Tyr-Val-Gly
Frog
-
pH 6.0, 37C, recombinant enzyme
0.9
N-[(2-phenylcyclopropyl)carbonyl]glycine
-
apparent KM
0.059
N-[(benzylmercapto)carbonyl]glycine
-
apparent KM
0.007
N-[3-(1-leucylpyrrolidin-2-yl)-3-oxopropanoyl]-L-phenylalanylglycine
-
pH and temperature not specified in the publication
0.55
N-[3-(1-leucylpyrrolidin-2-yl)-3-oxopropanoyl]glycylglycine
-
pH and temperature not specified in the publication
1.9
nicotinuric acid
-
apparent KM
0.17
O-acetyl-L-mandelyl-Gly
-
pH not specified in the publication, temperature not specified in the publication
0.1
O2
-
substrate N-decanoylglycine, pH 6.0, 37C
0.11
O2
-
substrate N-octanoylglycine, pH 6.0, 37C
0.15
O2
-
substrate N-hexanoylglycine, pH 6.0, 37C
0.17
O2
-
substrate N-butyrylglycine, pH 6.0, 37C
0.21
O2
-
substrate N-propionylglycine, pH 6.0, 37C
0.23
O2
-
substrate N-acetylglycine, pH 6.0, 37C
95.37
O2
-
protiated
658.1
O2
-
deuterated
0.009
peptidylglycine
-
transiently expressed mutants Q170N and Q170L, pH 5.5
0.01
peptidylglycine
-
transiently expressed mutant Q170E, pH 5.5
0.011
peptidylglycine
-
transiently expressed wild-type enzyme, pH 5.5
0.018
peptidylglycine
-
transiently expressed mutants Q170A and Y79W, pH 5.5
0.36
phenylhydantoic acid
-
apparent KM
0.19
phenylmercaptoacetylglycine
-
apparent KM
0.024
phenylthioacetylglycine
-
apparent KM
1.1
S-(1,2-dicarboxyethyl)-glutathione
-
pH 6.0, 37C
0.027
S-(4-nitrobenzyl)-glutathione
-
pH 6.0, 37C
0.067
S-butyl-glutathione
-
pH 6.0, 37C
0.016
S-decyl-glutathione
-
pH 6.0, 37C
0.23
S-ethyl-glutathione
-
pH 6.0, 37C
0.035
S-hexyl-glutathione
-
pH 6.0, 37C
0.27
S-methyl-glutathione
-
pH 6.0, 37C
0.032
S-octyl-glutathione
-
pH 6.0, 37C
0.11
S-propyl-glutathione
-
pH 6.0, 37C
3.7
tBOC-Gly
-
apparent KM
0.3
tBOC-Gly-Gly
-
apparent KM
0.0044
Trinitrophenyl-D-Tyr-Val-Gly
-
PC-3 TIS media
0.0068
Trinitrophenyl-D-Tyr-Val-Gly
-
DU-145 TIS media
0.6
ubiquitin
-
100 mM MES/NaOH, pH 6.0, 30 mM NaCl, 1% (v/v) ethanol, 0.001% (v/v) Triton X-100, 1 microM Cu(NO3)2, 10 mg/l catalase, 6 mM ascorbate, 8 microM N-dansyl-Tyr-Val-Gly
0.035
leukotriene C4
-
pH 6.0, 37C
additional information
additional information
-
Km for D-Tyr-Val-Gly depends on concentration of ascorbate, Km for ascorbate is constant over a wide range of D-Tyr-Val-Gly concentration
-
additional information
additional information
-
different assay methods
-
additional information
additional information
-
-
-
additional information
additional information
-
competitive and noncompetitive kinetic isotope effects in wild-type enzyme and mutant Y318F, kinetic mechanism
-
additional information
additional information
-
fluorescence spectroscopic analysis of intrinsic tryptophan
-
additional information
additional information
-
kinetics
-
additional information
additional information
-
reaction thermodynamics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.02
acetyl-Tyr-Phe-Gly
-
-
51
alpha-hydroxyhippuric acid
-
0.4 mM ferrocyanide, 100 mM MES pH 6.0, 30 mM KCl, 1 microM CuSO4
0.13
D-Tyr-Val-Gly
Frog
-
pH 7.5, 37C, recombinant enzyme
17
dansyl-Gly-Gly-Ser-CO-NH-CH2-COOH
-
pH 6.0, 37C, recombinant enzyme
0.08
dansyl-L-Tyr-L-Val-Gly
-
mutant enzyme H107A, in100 mM MES pH 5.5, at 37C
-
0.11
dansyl-L-Tyr-L-Val-Gly
-
mutant enzyme H108A, in100 mM MES pH 5.5, at 37C
-
4.6
dansyl-L-Tyr-L-Val-Gly
-
mutant enzyme M109I, in100 mM MES pH 5.5, at 37C
-
13.8
dansyl-L-Tyr-L-Val-Gly
-
wild type enzyme, in100 mM MES pH 5.5, at 37C
-
0.143
dansyl-Tyr-Val-Gly
-
-
0.983
dansyl-Tyr-Val-Gly
-
-
0.02
hippuric acid
Frog
-
pH 5.0, 37C, recombinant enzyme
13.6
hippuric acid
-
pH 6.0, 37C, [2H2]-hippuric acid, mutant Y318F
25
hippuric acid
-
pH 6.0, 37C, [2H2]-hippuric acid, wild-type enzyme
27.6
hippuric acid
-
pH 6.0, 37C, [1H2]-hippuric acid, mutant Y318F
39.1
hippuric acid
-
pH 6.0, 37C, [1H2]-hippuric acid, wild-type enzyme
0.0035
N-acetyl-Tyr-Val-Gly
-
purified recombinant mutant Y79W, pH 7.0
0.09
N-acetyl-Tyr-Val-Gly
-
purified recombinant mutant Y79W, pH 5.5
0.53
N-acetyl-Tyr-Val-Gly
-
purified recombinant wild-type enzyme, pH 7.0
0.62
N-acetyl-Tyr-Val-Gly
-
purified recombinant mutant Q170A, pH 7.0
14
N-acetyl-Tyr-Val-Gly
-
purified recombinant mutant Q170A, pH 5.5
15
N-acetyl-Tyr-Val-Gly
-
purified recombinant wild-type enzyme, pH 5.5
3
N-benzoylglycine
-
15C
14.5
N-benzoylglycine
-
37C
0.35
N-dansyl-Tyr-Val-Gly
P19021
pH 6.5, 37C
5
N-dansyl-Tyr-Val-Gly
-
-
1.4
N-trinitrophenyl-D-Tyr-Val-Gly
Frog
-
pH 6.0, 37C, recombinant enzyme
37
HOOC-NH-CH2-COOH
-
pH 6.0, 37C, recombinant enzyme
additional information
additional information
-
intrinsic rate constants for wild-type and mutant Y318F enzyme
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
46.8
N-dansyl-Tyr-Val-Gly
P19021
pH 6.5, 37C
16122
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.44
(2E)-4-oxo-4-phenylbut-2-enoic acid
-
pH 6.5, 37C
0.015
(3E)-4-(4-methoxyphenyl)but-3-enoic acid
-
pH 6.5, 37C
0.0057
(3E)-4-(4-methylphenyl)but-3-enoic acid
-
pH 6.5, 37C
0.0039
(3E)-4-[3-(benzyloxy)-4-methoxyphenyl]but-3-enoic acid
-
pH 6.5, 37C
0.019
(3E)-4-[4-(benzyloxy)phenyl]but-3-enoic acid
-
pH 6.5, 37C
7.9
(CBZ-hydrazido)glycine
-
Ki,s
75
(nicotinamidomethyl)phosphonic acid
-
Ki,s, larger than 75
0.06
(R)-5-acetamido-4-oxo-6-phenyl-2-hexenoic acid
-
pH 6.5, 37C
0.054
(S)-5-acetamido-4-oxo-6-phenyl-2-hexenoic acid
-
pH 6.5, 37C
0.057
(S)-5-acetamido-7-methylthio-4-oxo-2-heptenoic acid
-
pH 6.5, 37C
1.4
(S)-N-CBZ-4-amino-2-hydroxybutyric acid
-
Ki,s
2.9
3-benzoylpropionic acid
-
Ki,s
0.001
4-Phenyl-3-butenoic acid
-
strictly ascorbate dependent
0.019
4-Phenyl-3-butenoic acid
-
pH 6.5, 37C
0.0034
4-phenylbut-3-enoic acid
-
PC-3 TIS media
0.0057
4-phenylbut-3-enoic acid
-
DU-145 TIS media
0.035
6-O-palmitoyl-L-ascorbate
-
Ki,s
2.11
acetyl-D-Leu-OCH2COOH
-
-
1.3
acetyl-D-Phe-Gly
-
-
2.25
acetyl-D-Phe-OCH2COOH
-
-
0.522
acetyl-DL-Phe-OCH2COOH
-
-
1.25
acetyl-Gly-OCH2COOH
-
-
0.0598
acetyl-L-Leu-OCH2COOH
-
-
0.58
acetyl-L-Phe-D-Phe-Gly
-
-
0.002
acetyl-L-Phe-Gly
-
-
0.045
acetyl-L-Phe-OCH2COOH
-
-
0.005
adrenocorticotrophic hormone (1-10)
-
-
0.001
alpha-N-acetyl-adrenocorticotrophic hormone(1-14)
-
-
0.00113
diethyldithiocarbamate
-
DU-145 TIS media
0.00119
diethyldithiocarbamate
-
PC-3 TIS media
0.00051
Disulfiram
-
DU-145 TIS media
0.00065
Disulfiram
-
PC-3 TIS media
0.0006
endorphin(51-61)NH2
-
-
-
0.066
glutathione ethyl ester
-
Ki,s
0.015
glyoxylate phenylhydrazone
-
-
0.11
glyoxylate thiosemicarbazone
-
-
2.9
hippuric acid
-
pH 6.0, 37C, [1H2]-hippuric acid, wild-type enzyme
4.5
hippuric acid
-
pH 6.0, 37C, [2H2]-hippuric acid, wild-type enzyme
7
hippuric acid
-
pH 6.0, 37C, [2H2]-hippuric acid, mutant Y318F
22
hippuric acid
-
pH 6.0, 37C, [1H2]-hippuric acid, mutant Y318F
1.3
Monoethyl fumarate
-
-
0.069
N,S-dibenzoyl-L-cysteine
-
Ki,s
1.5
N-(benzoyl)-D-serine
-
Ki,s
0.0072
N-(thiobenzoyl)-(D,L)-alanine
-
Ki,s
2.1
N-acetyl-D-Leu-OCH2COOH
-
pH not specified in the publication, temperature not specified in the publication
1.3
N-acetyl-D-Phe-Gly
-
pH not specified in the publication, temperature not specified in the publication
0.0598
N-acetyl-L-Leu-OCH2COOH
-
pH not specified in the publication, temperature not specified in the publication
0.0452
N-acetyl-L-Phe-OCH2COOH
-
pH not specified in the publication, temperature not specified in the publication
18
N-benzylglycine
-
Ki,s
0.11
N-phenylthiohydantoic acid
-
Ki,s
0.054
O-(phenylcarbamoyl)glycolic acid
-
Ki,s
8.1
O-acetyl-D-mandelyl-Gly
-
pH not specified in the publication, temperature not specified in the publication
1
O-benzamidoglycolic acid
-
Ki,s
1
Pro-Leu-Gly hydroxamic acid
-
Ki,s
0.0079
S-(2-phenylthioacetyl)thioglycolic acid
-
Ki,s
0.0094
S-(3-phenylthiopropionyl)thioglycolic acid
-
Ki,s
0.0035
S-(4-methylthiobenzoyl)thioglycolic acid
-
Ki,s
0.11
S-(4-methylthiobenzoyl)thioglycolic acid ethyl ester
-
Ki,s
0.0026
S-(phenylthiocarbamoyl)-3-mercaptopropionic acid
-
Ki,s
0.0086
S-(phenylthiocarbamoyl)thioglycolic acid
-
Ki,s
0.058
S-(thiobenzoyl)-(R,S)-thiolactic acid
-
Ki,s
0.0057
S-(thiobenzoyl)-4-mercapto-4-cyanopentanoic acid
-
Ki,s
0.039
S-(thiobenzoyl)thioglycolic acid
-
Ki,s
0.00054
S-(thiolauroyl)thioglycolic acid
-
Ki,s
0.38
S-phenylmercaptoacetic acid
-
Ki,s
0.3
Salicylhydroxamic acid
-
Ki,s
0.16
trans-Benzoylacrylic acid
-
-
0.131
[(1R,2S)-2-phenylcyclopropyl]acetic acid
-
pH 6.5, 37C
0.48
[(4-Methoxybenzoyl)oxy]acetic acid
-
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.1
(acetyloxy)acetic acid
-
pH and temperature not specified in the publication
0.007
(decanoylsulfanyl)acetic acid
-
pH and temperature not specified in the publication
0.00006
(dodecanoyloxy)acetic acid
-
pH and temperature not specified in the publication
0.37
([(2S)-2-[(2-aminopropanoyl)amino]-3-phenylpropanoyl]oxy)acetic acid
-
pH and temperature not specified in the publication
0.038
([N-[3-(1-leucylpyrrolidin-2-yl)-3-oxopropanoyl]-L-phenylalanyl]oxy)acetic acid
-
pH and temperature not specified in the publication
0.18
([N-[3-(1-leucylpyrrolidin-2-yl)-3-oxopropanoyl]glycyl]oxy)acetic acid
-
pH and temperature not specified in the publication
0.29
([[(2S)-1-(2-aminopropanoyl)pyrrolidin-2-yl]carbonyl]oxy)acetic acid
-
pH and temperature not specified in the publication
1.1
([[(2S)-1-[[(2-aminopropanoyl)amino]acetyl]pyrrolidin-2-yl]carbonyl]oxy)acetic acid
-
pH and temperature not specified in the publication
0.2
([[(4-amino-6-methyl-3-oxoheptanoyl)amino]acetyl]oxy)acetic acid
-
pH and temperature not specified in the publication
0.000096
4-phenylbut-3-enoic acid
-
PC-3 TIS media
0.00068
4-phenylbut-3-enoic acid
-
DU-145 TIS media
0.00005
decanoyloxyacetic acid
-
pH and temperature not specified in the publication
0.000053
diethyldithiocarbamate
-
PC-3 TIS media
0.00011
diethyldithiocarbamate
-
DU-145 TIS media
0.002
[(phenylacetyl)oxy]acetic acid
-
pH and temperature not specified in the publication
0.045
[(phenylacetyl)sulfanyl]acetic acid
-
pH and temperature not specified in the publication
-
0.006
[[(2S)-2-(acetylamino)-3-phenylpropanoyl]oxy]acetic acid
-
pH and temperature not specified in the publication
0.011
[[(2S)-2-(acetylamino)-3-phenylpropanoyl]oxy]acetic acid
-
pH and temperature not specified in the publication
0.045
[[(2S)-2-(acetylamino)-3-phenylpropanoyl]sulfanyl]acetic acid
-
pH and temperature not specified in the publication
0.16
[[(2S)-2-([[(2-aminopropanoyl)amino]acetyl]amino)-3-phenylpropanoyl]oxy]acetic acid
-
pH and temperature not specified in the publication
1.6
[[(2S)-2-amino-3-phenylpropanoyl]oxy]acetic acid
-
pH and temperature not specified in the publication
0.5
[[(2S)-pyrrolidin-2-ylcarbonyl]oxy]acetic acid
-
pH and temperature not specified in the publication
1.8
[[(acetylamino)acetyl]oxy]acetic acid
-
pH and temperature not specified in the publication
0.009
[[N-(4-amino-6-methyl-3-oxoheptanoyl)-L-phenylalanyl]oxy]acetic acid
-
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0000000004
-
H9c2 cells
0.000000112
-
PHM activity, normoxia, medulla, dorsal
0.000000155
-
PAM activity, normoxia, control
0.0000002
-
PHM activity, normoxia, medulla, ventral
0.000000202
-
PHM activity, normoxia, control
0.000000207
-
PAM activity, continuous hypobaric hypoxia, 10 days
0.000000222
-
PHM activity, normoxia, pons, ventral
0.000000268
-
PAM activity, intermittent hypoxia, 1 day
0.000000298
-
PHM activity, intermittent hypoxia, 1 day
0.000000312
-
PHM activity, intermittent hypoxia, medulla, dorsal
0.000000315
-
PHM activity, continuous hypobaric hypoxia, 10 days
0.000000578
-
PHM activity, intermittent hypoxia, 3 days
0.000000648
-
PHM activity, intermittent hypoxia, 10 days
0.00000066
-
PAM activity, intermittent hypoxia, 3 days
0.000000667
-
PHM activity, normoxia, pons, dorsal
0.0000008
-
PHM activity, intermittent hypoxia, medulla, ventral
0.000000888
-
PHM activity, intermittent hypoxia, ventral
0.000000907
-
PAM activity, intermittent hypoxia, 10 days
0.0000016
-
PHM activity, intermittent hypoxia, pons, dorsal
0.000012
-
PAM+/- mouse, POA, hypothalamus
0.000015
-
PAM+/- mouse, PVN, hypothalamus
0.000037
-
wild-type mouse, POA, hypothalamus
0.00004
-
wild-type mouse, PVN, hypothalamus
0.000043
-
PAM+/- mouse, pituitary
0.00008
-
wild-type mouse, pituitary
0.0014
-
pH 6.5, 37C
0.0033
-
alpha-amidating lyase activity
0.01
-
N-dansyl-Tyr-Val-Gly
0.0124
-
skin, peptidylhydroxylglycine N-C lyase, highest activity of all tissues
0.0206
-
skin, peptidylglycine alpha-hydroxylating activity, highest activity of all tissues
0.038
-
purified PAM-A
0.115
-
purified PAM-B
0.53
P19021
purified recombinant enzyme, peptidylglycine alpha-hydroxylating monooxygenase activity
0.85
Frog
-
purified recombinant enzyme, substrate N-trinitrophenyl-D-Tyr-Val-Gly
1.15
-
recombinant purified enzyme
1.15
-
-
2.07
-
purified enzyme
3
-
purified recombinant enzyme
5.9
-
purified recombinant enzyme
16
-
purified recombinant enzyme
additional information
-
-
additional information
-
very low activity in crude subcellular preparations
additional information
-
very low activity in crude subcellular preparations
additional information
-
-
additional information
-
-
additional information
-
peptidylglycine alpha-amidating and alpha-hydroxylating monooxygenase activities in several tumor tissue extracts, comparison with immunological analysis, overview, highest activity in medullary thyroid carcinoma
additional information
-
-
additional information
-
very low activity in H9c2 cells, no ascorbate in assay mixture
additional information
-
-
additional information
Frog
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 4.5
-
membrane-bound peptidylglycine-alpha-hydroxylating activity
4.5 - 5
-
recombinant enzyme
4.5 - 5
-
soluble peptidylglycine-alpha-hydroxylating activity
5
-
assay at
5
Frog
-
with substrate hippuric acid
5.4
-
assay at, recombinant enzyme
5.5 - 6
-
-
5.5 - 7
-
assay at
5.8
-
the enzyme undergoes loss of activity at lower pHs due to a protonation
6 - 7
P19021
assay at, dependent on the substrate used
6
-
2 optima: at pH 6.0 and at pH 7.5
6
-
MES buffer, recombinant from 1, AE-I
6
Frog
-
with substrate N-trinitrophenyl-D-Tyr-Val-Gly
6
-
activity assay
6
-
activity assay; assay at
6.5 - 7.5
-
-
6.5
-
activity assay
6.5
P19021
assay at
7 - 8
-
dependent on Cu2+-concentration
7
-
assay at, recombinant enzyme
7
-
phosphate buffer, recombinant form 1, AE-I
7.5
-
-
7.5
-
2 optima: at pH 6.0 and at pH 7.5
7.5
Frog
-
with substrate D-Tyr-Val-Gly
8.5
-
PAM-A
8.5
-
-
9 - 9.5
-
PAM-B
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 9
-
recombinant enzyme
6 - 7.5
-
about 70% of activity maximum at pH 6.0 and 7.5
7.5 - 10
-
pH 7.5: about 50% of activity maximum, pH 10: about 60% of activity maximum, PAM-B
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
-
assay at
37
Frog
-
assay at
37
-
assay at
37
-
activity assay
37
-
activity assay; assay at
37
-
activity assay
37
-
activity assay
37
P19021
assay at
additional information
-
above 40C, temperature dependence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
predominantly membrane-associated, bifunctional enzyme
Manually annotated by BRENDA team
Q4W7B5
neuronal cell bodies, axon bundles
Manually annotated by BRENDA team
Q4W7B5
expression only in the photoreceptor cells adjacent to the eye cup
Manually annotated by BRENDA team
-
abdominal and pleuropedal
Manually annotated by BRENDA team
-
predominantly membrane-associated, bifunctional enzyme
Manually annotated by BRENDA team
-
myoblast, H9c2 cells
Manually annotated by BRENDA team
-
atrium, ventricle
Manually annotated by BRENDA team
-
peptidylglycine monooxygenase from the HL-1 cell line shows a 5fold higher specific activity compared to the enzyme from rat atrium
Manually annotated by BRENDA team
-
2 forms, distinguishable by molecular weight
Manually annotated by BRENDA team
-
atrial myocyte
Manually annotated by BRENDA team
-
anterior, intermediate and posterior
Manually annotated by BRENDA team
-
peptidylglycine alpha-amidating monooxygenase activity in copper-deficient lactating dams is reduced to 15% compared to controls. Pups fed by copper-deficient dams showed an earlier decrease of peptidylglycine alpha-amidating monooxygenase activity throughout lactation
Manually annotated by BRENDA team
-
soluble enzyme with peptidylglycine alpha-hydroxylating activity, AE-I
Manually annotated by BRENDA team
-
soluble enzyme with peptidylglycine alpha-hydroxylating activity or peptidylhydroxylglycine N-C lyase activity
Manually annotated by BRENDA team
additional information
-
tissue distribution, overview
Manually annotated by BRENDA team
additional information
-
tissue distribution, overview
Manually annotated by BRENDA team
additional information
-
enzyme expression level in different tissues in copper adequate and deficient status, overview
Manually annotated by BRENDA team
additional information
Q4W7B5
tissue expression pattern, the enzyme colocalizes with cytochrome b561 along the central nervous system
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
peptidylglycine alpha-hydroxylating activity and peptidylhydroxylglycine N-C lyase activity
Manually annotated by BRENDA team
-
recombinant enzyme secreted into medium
-
Manually annotated by BRENDA team
-
transmembranal protein
Manually annotated by BRENDA team
-
integral membrane
Manually annotated by BRENDA team
-
recombinant bifunctional enzyme form 2, uncleaved in insect cells
Manually annotated by BRENDA team
-
from neurosecretory vesicles
Manually annotated by BRENDA team
-
particulate form, except for abdominal ganglia
Manually annotated by BRENDA team
-
chromaffin granules
Manually annotated by BRENDA team
-
chromaffin granules
Manually annotated by BRENDA team
-
synaptosomal and neurosecretory granules
Manually annotated by BRENDA team
-
from atrial myocytes, enzyme is recruited by aggregates of pro-atrial natriuretic peptide proANP, N-terminally deleted proANP is inhibited in recruiting the enzyme
Manually annotated by BRENDA team
-
transmembrane protein with lumenal and cytoplasmic parts, overview, abundant in atrial secretory vesicles
Manually annotated by BRENDA team
additional information
-
distribution of membrane-bound and soluble peptidylglycine alpha-hydroxylating activity
-
Manually annotated by BRENDA team
additional information
Q4W7B5
localization around the nuclei
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35000
-
PHM, proteolytic processed, determined by SDS-PAGE and Western blot analysis
698532
35040
-
MALDI-MS, recombinant enzyme
676976
38000
-
PAM-B, heterogeneous in size, gel filtration
438570
39000
-
native wild-type enzyme; SDS-PAGE, gel filtration
438569
39000
-
SDS-PAGE, gel filtration
438573
40000
-
gel fltration, SDS-PAGE
438563
42000
-
PHM, determined by SDS-PAGE and Western blot analysis
698532
43000
-
recombinant wild-type enzyme, SDS-PAGE, gel filtration
438569
43000
-
recombinant form B, gel filtration and SDS-PAGE
438571
49000
-
form 1, gel filtration
438582
50000
-
gel filtration
438562
54000
-
PAM-A, heterogeneous in size, gel filtration
438570
60000
-
gel filtration; shows reversible aggregation with MW of 100000
438564
60000
-
gel filtration
438586
69000
-
form 2, gel filtration
438582
75000
-
recombinant from mouse cells, gel filtration
438566
75000
-
recombinant form A, gel filtration and SDS-PAGE
438571
75000
-
gel filtration and native PAGE
438574
75000
-
recombinant form A, gel filtration and SDS-PAGE
438589
78000
-
recombinant mutant AE-II, form 2, gel filtration
438584
87000
-
determined by SDS-PAGE and Western Blot analysis
697630
92000
-
gel filtration
438579
95000
-
gel filtration
673155
100000
-
PAM, determined by SDS-PAGE and Western blot analysis
699036
additional information
-
-
438567
additional information
-
-
438587
additional information
-
PAM in particulate fraction of H9c2 cells contains 86, 76, and 46 kDa proteins, soluble PAM fraction contains 110, 86, and 46 kDa proteins
438588
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 75000, SDS-PAGE
?
-
x * 125000, PAM-1, SDS-PAGE, x * 110000, PAM-2, SDS-PAGE, x * 90000, PAM-3, SDS-PAGE
?
Frog
-
x * 40000, recombinant enzyme, SDS-PAGE
?
P19021
x * 91000, recombinant soluble enzyme, SDS-PAGE
monomer
-
1 * 40000, SDS-PAGE
monomer
-
1 * 75000, SDS-PAGE
monomer
-
1 * 39000, SDS-PAGE
monomer
-
1 * 92000, SDS-PAGE
monomer
-
1 * 75000, type A, SDS-PAGE
monomer
-
1 * 75000, recombinant enzyme, SDS-PAGE
monomer
-
1 * 38000, PAM-B, heterogeneous in size, SDS-PAGE
monomer
-
1 * 43000, type B, SDS-PAGE
monomer
-
1 * 48000, PAM-A, heterogeneous in size, SDS-PAGE
monomer
-
1 * 50000, membrane-bound form, SDS-PAGE
monomer
-
1 * 74000, recombinant mutant AE-II, form 2, SDS-PAGE
additional information
-
enzyme PAM-1, the longest transcript, is composed of, at the lumenal side, the peptidylglycine alpha-hydroxylating monooxygenase PHM catalytic domain, a noncatalytic domain from exon A, the peptidyl-alpha-hydroxyglacine alpha-amidating lyase PAL catalytic domain, a transmembrane domain, and a C-terminal cytoplasmic domain, deletion of exon A yields PAM-2, further deletion of the transmembrane domain yields soluble PAM-3 within the vesicle lumen
additional information
P19021
the enzyme possesses 2 catalytic domains
additional information
P19021
the specific components of the thioredoxin-hPHMcc-His6 fusion protein are as follows: 11.8 kDa for thioredoxin, 5.9 kDa peptide between thioredoxin and hPHMcc, 35.2 kDa for hPMHcc, a 1.5 kDa peptide on the C-terminal side of hPHMcc, and 0.6 kDa for the His6 tag. The sum of the individual masses are 55 kDa, in agreement with the 52 kDa measure by SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
P19021
enzyme contains 2 putative N-glycosylation sites at ASn411 and Asn762, the purified enzyme contains at least 1 sugar chain
glycoprotein
-
partially glycosylated, at Asn 660, recombinant enzyme from mouse cells
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging-drop diffusion method at 293 K
-
molecular dynamics simulations based onthe crystal structure 1SDW, overview
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
rapid inactivation of recombinant enzyme at acidic pH in vitro
438566
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4
-
incubation for 12-15 h, 47% loss of activity
438562
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Cu2+ can restore EDTA-treated only the alpha-hydroxylating activity
-
repeated freeze-thaw cycles have no effect on enzyme activity
-
substance-P, i.e. RPKPQQFFGLM-NH2, protects against inactivation by sulfite
-
stabilized by salts like KI and KCl, recombinant form 1, AE-I
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
membrane-bound form from atrial gland
-
forms A and B differing in MW and charge
-
peptidylglycine alpha-hydroxylating monooxygenase and a peptidyl-alpha-hydroxyglycine alpha-amidating lyase
-
recombinant enzyme from CHO cell culture medium by copper-chelating affinity chromatography
Frog
-
cell extracts are prepared
-
Poros 20 m HQ anion exchange resin column chromatography
-
recombinant soluble enzyme from culture medium in a 3-step chromatographic procedure, about 40fold to near homogeneity
P19021
thioredoxin-hPHMcc-His6 fusion is purified to homogeneity
P19021
large scale purification of the recombinant truncated enzyme, comprising the catalytic core residues 42-356, from CHO DG44 cells, reconstitution of copper bound to the enzyme; two chromatoography steps
-
mutant H172A of type A alpha-AE, recombinant from chinese hamster ovary cells
-
recombinant from mouse cells
-
recombinant from mouse cells; type A and B
-
recombinant wild-type and mutant enzymes from CHO cells by a 3-step chromatographic method
-
two chromatography steps
-
two chromatoography steps
-
type A alpha-AE, recombinant from chinese hamster ovary cells
-
membrane bound form
-
cation-exchange chromatography, anion-exchange chromatography, gel filtration
-
native wild-type and recombinant from Spodoptera frugiperda cell expression system
-
truncated mutant form 2 from gene AE-II, recombinant from Spodoptera frugiperda cell expression system
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Drosophila S2 cells
-
stable and functional expression in CHO cells, method establishment, induction of enzyme expression by addition of sodium propionate, N,N'-hexamethylene-bis-acetamide, or best by sodium butyrate, recombinant enzyme is mostly excreted to the medium
Frog
-
expressed in CHO cells
-
expressed in CHO DG44 cells
-
production of the catalytic core of human peptidylglycine alpha-hydroxylating monooxygenase (hPHMcc) in Escherichia coli possessing a N-terminal fusion to thioredoxin. Thioredoxin is fused to hPHMcc to enhance the yield of the resulting 52 kDa protein as a soluble and catalytically active enzyme
P19021
subcloning from human heart lambda-gt10 library in Escherichia coli, soluble recombinant enzyme through elimination of the C-terminal membrane-spanning domain, expression of a soluble form in CHO K-1 cells, excretion of the recombinant enzyme to the cell culture medium
P19021
expressed in CHO cells
-
DNA and amino acid sequence determination and analysis, phylogenetic analysis
Q4W7B5
expression in CHO cells
-
expression in CHO DG44 cells
-
expression in CHO DG44 cells; expression of the truncated enzyme, comprising the catalytic core residues 42-356, in CHO DG44 cells
-
medullary thyroid alpha-AE, type A, expression in chinese hamster ovary cells
-
medullary thyroid carcinoma enzyme, expression in mouse C 127 cells via bovine papilloma virus vector, amino acid and DNA sequence analysis
-
myoblast enzyme, expression in H9c2 cells
-
single copy gene, alternative splicing generates several forms of enzyme mRNA, overview
-
transient expression of wild-type and mutant enzymes in HEK293 cells, stable expression of wild-type and mutant enzymes in CHO cells
-
truncated type A enzyme, expression in mouse C127 cells
-
truncated version (residues 42-356) expressed in CHO cell
-
expressed in Sf9 cell
-
expression in Spodoptera fugiperda cells via baculovirus vector of membrane-associated, bifunctional enzyme form 2, AE-II, wild-type and truncated mutant, N-terminal amino acid sequence analysis
-
expression in Spodoptera fugiperda cells via baculovirus vector of membrane-associated, bifunctional enzyme form 2, AE-III
-
expression in Spodoptera fugiperda cells via baculovirus vector of soluble form 1, AE-I showing only peptidylglycine alpha-hydroxylating activity
-
expression in Spodoptera fugiperda cells via baculovirus vector, amino acid sequence analysis
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
intermittent hypoxia activates peptidylglycine alpha-amidating monooxygenase via reactive oxygen species-mediated proteolytic processing
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H172A
-
coppper biniding similar to wild type, but showed a 1000fold decrease in turnover rate
H107A
-
low activity
H108A
-
low activity
M109I
-
low activity
M314H
-
the catalytic activity of the mutant decreases by 96% due to effects on both kcat and KM but it displayed the same activity/pH profile with a maximum around pH 6.0
H172A
-
mutant of copper ligand of peptidylglycine alpha-hydroxylating enzyme, reduced copper content below 0.3 Cu2+ per protein molecule
H172A
-
mutation in the copper center of domain one, no activity in presence of H2O2
Q170A
-
site-directed, PCR-based mutagenesis, altered Km compared to the wild-type enyme
Q170A
-
site-directed mutagenesis, mutant enzyme activity as a function of the number of hydrogen bonds established in the bridge between the two copper ions compared to the wild-type enzyme
Q170E
-
site-directed, PCR-based mutagenesis, kinetics similar to the wild-type enyme
Q170E
-
site-directed mutagenesis, mutant enzyme activity as a function of the number of hydrogen bonds established in the bridge between the two copper ions compared to the wild-type enzyme
Q170L
-
site-directed, PCR-based mutagenesis, kinetics similar to the wild-type enyme
Q170L
-
site-directed mutagenesis, mutant enzyme activity as a function of the number of hydrogen bonds established in the bridge between the two copper ions compared to the wild-type enzyme
Q170N
-
site-directed, PCR-based mutagenesis, kinetics similar to the wild-type enyme
Q170N
-
site-directed mutagenesis, mutant enzyme activity as a function of the number of hydrogen bonds established in the bridge between the two copper ions compared to the wild-type enzyme
Y318F
-
site-directed mutagenesis, active site residue mutant, slightly reduced rate constant for C-H bond cleavage compared to the wild-type enzyme
Y79W
-
site-directed, PCR-based mutagenesis, altered kinetics compared to the wild-type enzyme, highly reduced activity
H242A
-
mutation in the copper center of domain two, no activity in presence of H2O2
additional information
-
only the residues 42-356 carrying the monoogenase domain was expressed
additional information
-
large scale production of the enzyme using an automated bioreactor, method optimization and evaluation, overview
additional information
-
protein containing residues 42-356
Y79W
-
site-directed mutagenesis, mutant enzyme activity as a function of the number of hydrogen bonds established in the bridge between the two copper ions compared to the wild-type enzyme
additional information
-
construction of a truncated form of AE-II, lacking the transmembrane domain and leading to solubility of the fully active, truncated enzyme being secreted into the culture medium from Spodoptera frugiperda cells
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
PHM is a potential target for the development of insecticides
medicine
-
enzyme is an attractive target for anti-tumor compounds
medicine
-
PHM is a potential target for the development of inhibitors as drugs for the teratment of human disease
medicine
-
PHM is a potential target for the development of inhibitors as drugs for the treatment of human disease
pharmacology
-
enzyme is an attractive target for development of anti-tumor compounds